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Entry version 88 (03 Jul 2019)
Sequence version 2 (01 May 2007)
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Protein

Collagen alpha-1(II) chain

Gene

col2a1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1300CalciumBy similarity1
Metal bindingi1302CalciumBy similarity1
Metal bindingi1303Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1305Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1308CalciumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagen alpha-1(II) chainBy similarity
Alternative name(s):
Alpha-1 type II collagenBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:col2a1By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-6252613 col2a1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 26Sequence analysisAdd BLAST26
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000028617827 – 183N-terminal propeptideBy similarityAdd BLAST157
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000286179184 – 1243Collagen alpha-1(II) chainAdd BLAST1060
PropeptideiPRO_00002861801244 – 1486C-terminal propeptideBy similarityAdd BLAST243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei6614-hydroxyprolineBy similarity1
Modified residuei6704-hydroxyprolineBy similarity1
Modified residuei6723-hydroxyprolineBy similarity1
Modified residuei6734-hydroxyprolineBy similarity1
Modified residuei6764-hydroxyprolineBy similarity1
Modified residuei9104-hydroxyprolineBy similarity1
Modified residuei9164-hydroxyprolineBy similarity1
Modified residuei9224-hydroxyprolineBy similarity1
Modified residuei11463-hydroxyprolineBy similarity1
Modified residuei11883-hydroxyprolineBy similarity1
Modified residuei11894-hydroxyprolineBy similarity1
Modified residuei12033-hydroxyprolineBy similarity1
Modified residuei12044-hydroxyprolineBy similarity1
Modified residuei12074-hydroxyprolineBy similarity1
Modified residuei12093-hydroxyprolineBy similarity1
Modified residuei12104-hydroxyprolineBy similarity1
Modified residuei12134-hydroxyprolineBy similarity1
Modified residuei12153-hydroxyprolineBy similarity1
Modified residuei12164-hydroxyprolineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi1282 ↔ 1314PROSITE-ProRule annotation
Disulfide bondi1288Interchain (with C-1305)PROSITE-ProRule annotation
Disulfide bondi1305Interchain (with C-1288)PROSITE-ProRule annotation
Disulfide bondi1322 ↔ 1484PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi1387N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1392 ↔ 1437PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains.By similarity
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.By similarity
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.By similarity
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei183 – 184Cleavage; by procollagen N-endopeptidaseBy similarity2
Sitei1243 – 1244Cleavage; by procollagen C-endopeptidaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q91717

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Initially, the transcripts are localized to notochord, somites, and the dorsal region of the lateral plate mesoderm. At later stages of development and parallel to increased mRNA accumulation, collagen expression becomes progressively more confined to chondrogenic regions of the tadpole.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimers of alpha 1(II) chains.

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q91717

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini36 – 94VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1252 – 1486Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni203 – 1216Triple-helical regionAdd BLAST1014
Regioni1217 – 1243Nonhelical region (C-terminal)Add BLAST27

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K19719

Database of Orthologous Groups

More...
OrthoDBi
337699at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 8 hits
PF00093 VWC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q91717-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSFVDSRTL VLFAATQVIL LAVVRCQDEE DVLDTGSCVQ HGQRYSDKDV
60 70 80 90 100
WKPEPCQICV CDTGTVLCDD IICEESKDCP NAEIPFGECC PICPTEQSST
110 120 130 140 150
SSGQGVLKGQ KGEPGDIKDV LGPRGPPGPQ GPSGEQGSRG ERGDKGEKGA
160 170 180 190 200
PGPRGRDGEP GTPGNPGPVG PPGPPGLGGN FAAQMTGGFD EKAGGAQMGV
210 220 230 240 250
MQGPMGPMGP RGPPGPTGAP GPQGFQGNPG EPGEPGAGGP MGPRGPPGPS
260 270 280 290 300
GKPGDDGEAG KPGKSGERGP PGPQGARGFP GTPGLPGVKG HRGYPGLDGA
310 320 330 340 350
KGEAGAAGAK GEGGATGEAG SPGPMGPRGL PGERGRPGSS GAAGARGNDG
360 370 380 390 400
LPGPAGPPGP VGPAGAPGFP GAPGSKGEAG PTGARGPEGA QGPRGESGTP
410 420 430 440 450
GSPGPAGASG NPGTDGIPGA KGSSGGPGIA GAPGFPGPRG PPGPQGATGP
460 470 480 490 500
LGPKGQTGDP GVAGFKGEQG PKGEIGSAGP QGAPGPAGEE GKRGARGEPG
510 520 530 540 550
AAGPNGPPGE RGAPGNRGFP GQDGLAGPKG APGERGVPGL GGPKGGNGDP
560 570 580 590 600
GRPGEPGLPG ARGLTGRPGD AGPQGKVGPS GASGEDGRPG PPGPQGARGQ
610 620 630 640 650
PGVMGFPGPK GANGEPGKAG EKGLVGAPGL RGLPGKDGET GSQGPNGPAG
660 670 680 690 700
PAGERGEQGP PGPSGFQGLP GPPGSPGEGG KPGDQGVPGE AGAPGLVGPR
710 720 730 740 750
GERGFPGERG SSGPQGLQGP RGLPGTPGTD GPKGASGPSG PNGAQGPPGL
760 770 780 790 800
QGMPGERGAA GISGPKGDRG DTGEKGPEGA SGKDGSRGLT GPIGPPGPAG
810 820 830 840 850
PNGEKGESGP SGPPGIVGAR GAPGDRGENG PPGPAGFAGP PGADGQSGLK
860 870 880 890 900
GDQGESGQKG DAGAPGPQGP SGAPGPQGPT GVFGPKGARG AQGPAGATGF
910 920 930 940 950
PGAAGRVGTP GPNGNPGPPG PPGSAGKEGP KGVRGDAGPP GRAGDPGLQG
960 970 980 990 1000
AAGAPGEKGE PGEDGPSGPD GPPGPQGLSG QRGIVGLPGQ RGERGFPGLP
1010 1020 1030 1040 1050
GPSGEPGKQG GPGSSGDRGP PGPVGPPGLT GPSGEPGREG NPGSDGPPGR
1060 1070 1080 1090 1100
DGATGIKGDR GETGPLGAPG APGAPGAPGS VGPTGKQGDR GESGPQGPLG
1110 1120 1130 1140 1150
PSGPAGARGL AGPQGPRGDK GEAGEAGERG QKGHRGFTGL QGLPGPPGSA
1160 1170 1180 1190 1200
GDQGATGPAG PAGPRGPPGP VGPSGKDGSN GISGPIGPPG PRGRSGETGP
1210 1220 1230 1240 1250
SGPPGQPGPP GPPGPPGPGI DMSAFAGLSQ PEKGPDPMRY MRADQASNSL
1260 1270 1280 1290 1300
PVDVEATLKS LNNQIENIRS PDGTKKNPAR TCRDLKLCHP EWKSGDYWID
1310 1320 1330 1340 1350
PNQGCTVDAI KVFCDMETGE TCVYPNPSKI PKKNWWSAKG KEKKHIWFGE
1360 1370 1380 1390 1400
TINGGFQFSY GDDSSAPNTA NIQMTFLRLL STDASQNITY HCKNSIAFMD
1410 1420 1430 1440 1450
EASGNLKKAV LLQGSNDVEI RAEGNSRFTY NALEDGCKKH TGKWSKTVIE
1460 1470 1480
YRTQKTSRLP IVDIAPMDIG GADQEFGVDI GPVCFL
Length:1,486
Mass (Da):142,263
Last modified:May 1, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i02C18E5F5807100E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti456Q → E in AAA49678 (PubMed:1918153).Curated1
Sequence conflicti1287L → I in AAA49678 (PubMed:1918153).Curated1
Sequence conflicti1315D → N in AAA49678 (PubMed:1918153).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M63595 mRNA Translation: AAA49678.1
BC048221 mRNA Translation: AAH48221.1
BC111515 mRNA Translation: AAI11516.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A40333
B40333

NCBI Reference Sequences

More...
RefSeqi
NP_001081258.1, NM_001087789.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397738

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:397738

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63595 mRNA Translation: AAA49678.1
BC048221 mRNA Translation: AAH48221.1
BC111515 mRNA Translation: AAI11516.1
PIRiA40333
B40333
RefSeqiNP_001081258.1, NM_001087789.1

3D structure databases

SMRiQ91717
ModBaseiSearch...

Proteomic databases

PRIDEiQ91717

Genome annotation databases

GeneIDi397738
KEGGixla:397738

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
397738
XenbaseiXB-GENE-6252613 col2a1

Phylogenomic databases

KOiK19719
OrthoDBi337699at2759

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 8 hits
PF00093 VWC, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO2A1_XENLA
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q91717
Secondary accession number(s): Q7ZTI6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: July 3, 2019
This is version 88 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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